The main foci of research have been on the theory of protein folding and on the role of entropy barriers in determining reaction rates. One investigation was a critical analysis of "Levinthal's paradox". The paradox is that a random search through possible conformations of an unfolded protein will take cosmological times to arrive at the native structure. It was shown that this time can be reduced to a biologically significant size merely by including a small bias, of the order of a few kT, in factor of locally native conformations. Another investigation dealt with diffusion through geometrical bottlenecks. It was found that this could be described with moderate success as diffusion past entropy barriers instead of the more commonly used potential energy barriers. A third investigation was motivated by experimental observations on the viscosity dependence of ligand binding to myoglobin. It was found that a temporally fluctuating entropy bottleneck can explain some aspects of these experiments.